5WMN
Crystal Structure of HLA-B7 in complex with SPI, an influenza peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-02-08 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.954 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 69.396, 84.262, 77.945 |
| Unit cell angles | 90.00, 104.00, 90.00 |
Refinement procedure
| Resolution | 36.810 - 1.820 |
| R-factor | 0.1859 |
| Rwork | 0.184 |
| R-free | 0.22160 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3vcl |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.060 |
| Data scaling software | Aimless (0.3.11) |
| Phasing software | PHASER |
| Refinement software | BUSTER |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 47.610 | 47.610 | 1.860 |
| High resolution limit [Å] | 1.820 | 9.100 | 1.820 |
| Rmerge | 0.049 | 0.018 | 0.731 |
| Total number of observations | 292026 | 1931 | 16080 |
| Number of reflections | 77499 | 615 | 4402 |
| <I/σ(I)> | 19.8 | 67.5 | 2.1 |
| Completeness [%] | 99.3 | 93.1 | 96.1 |
| Redundancy | 3.8 | 3.1 | 3.7 |
| CC(1/2) | 0.999 | 0.999 | 0.769 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 277 | 18-24%PEG4000, 0.2 NH4 Acetate, 0.1M Na-cacodylate pH 6.5 |
